2.3.1.1: amino-acid N-acetyltransferase
This is an abbreviated version!
For detailed information about amino-acid N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.1
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2.3.1.1
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ammonia
-
hyperammonemia
-
ornithine
-
l-arginine
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citrulline
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carbamylphosphate
-
ureagenesis
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transcarbamylase
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carglumic
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accoa
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6.3.4.16
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gcn5-related
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protein-restricted
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carbamylglutamate
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nagks
-
feedback-resistant
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phenylbutyrate
-
ureotelic
-
analysis
-
medicine
- 2.3.1.1
- ammonia
-
hyperammonemia
- ornithine
- l-arginine
- citrulline
- carbamylphosphate
-
ureagenesis
-
transcarbamylase
-
carglumic
- accoa
-
6.3.4.16
-
gcn5-related
-
protein-restricted
- carbamylglutamate
-
nagks
-
feedback-resistant
- phenylbutyrate
-
ureotelic
- analysis
- medicine
Reaction
Synonyms
acetylglutamate synthase, acetylglutamate synthetase, acetylglutamic synthetase, acetyltransferase, amino acid, AGAS, amino acid acetyltransferase, ARG2, ArgA, ArgH(A), argJ, Cg3035, More, N-acetyl-glutamate synthase, N-acetyl-L-glutamate synthase, N-acetyl-L-glutamate synthase/kinase, N-acetyl-L-glutamate synthetase, N-acetylglutamate synthase, N-acetylglutamate synthase/kinase, N-acetylglutamate synthetase, NAGS, NAGS-K, NAGS/K, NAT, ngNAGS, PaNAGS, pitax, Rv2747, SINAGS1, XcNAGS
ECTree
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Molecular Weight
Molecular Weight on EC 2.3.1.1 - amino-acid N-acetyltransferase
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20978
21000
263000
tetrameric structure in the presence and absence of L-arginine, gel fitlration and ultracentrifugation
277000
-
tetramer-octamer equilibrium that shifts towards tetramers upon binding of L-arginine, gel fitlration and ultracentrifugation
37200
37400
38800
catalytic N-acetyltransferase domain, calculated from amino acid sequence
51700
-
6 * 51700, SDS-PAGE, cross-linking studies with dimethylsuberimidate, in the maximally aggregated state the enzyme exists as a hexamer
CAF20762, Q8NM40
x * 37200, calculated from amino acid sequence
37400
recombinant dimeric N-acetyltransferase domain, gel filtration